The adsorption behavior of quaternary ammonium cationic surfactants with different hydrocarbon chain lengths, i.e. HDTMA (hexadecyltrimethylammonium), TDTMA (tetradecyltrimethylammonium) and DDTMA (dodecyltrimethylammonium), onto clinoptilolite has been investigated. The adsorption isotherms of these surfactants are correlated with the ζ potential curves of clinoptilolite. Accordingly, the applicability of the hemimicelle hypothesis to the adsorption of cationic surfactants at the clinoptilolite/water interface considering in the electrical double layer (EDL) of clinoptilolite is discussed. Even though the adsorption occurs in the EDL of clinoptilolite, the adsorption of HDTMA, TDTMA and DDTMA onto clinoptilolite is not conveniently described by the hemimicelle hypothesis. The absence of all expected marked increase in the ζ potential curves at the hemimicelle concentration is ascribed to the large external cation exchange capacity of clinoptilolite. The hydrocarbon chain length of surfactant molecules is found to have a significant effect on the ion exchange as well as hydrophobic interaction mechanisms. The effectiveness of both ion exchange and hydrophobic interactions increases with increasing chain length, and so the greatest surfactant adsorption onto clinoptilolite was obtained by HDTMA.

Hydrophobic forces are known to have a crucial part not only in the conformation of the three-dimensional structure of proteins, but also in the build-up of DNA–protein complexes. Electric forces also play an important role both in the tertiary as well in the quaternary structure of macromolecular associations. Sometimes both hydrophobic and electric interactions add up their strengths to accomplish these structures but in most cases they act in opposite directions. This fact, together with being overall interactions with different ranges, provides a nuanced equilibrium also modulated by the need to comply with steric hindrances and geometric frustration effects. This review focuses on the utility of using the hydrophobic and electrical dipole moment vectors to describe the interactions that give rise to the structures of biological macromolecules. Although different definitions of both electric dipole and hydrophobic moments have been described in the literature, results obtained in biological assemblies demonstrate the principle of the biological membrane model. According to this model, postulated by our group, biological macromolecules tend to associate by aligning their hydrophobic moments in a similar manner to phospholipids in a membrane. Examples of both closed and open structures are used to assess the predictability of our model. We seek agreement between our results with those described in the current literature. The review ends with possible future projections using this formalism.

The effects of a bovine whey peptide product enriched in proline (wPRP) on the solubility of milk proteins were tested under ambient conditions or following heat treatment at 75 and 100 °C, for 1 and 15 min, followed by post-incubation storage at either ambient temperature or 4 °C for up to 7 d. wPRP promoted solubilisation of milk proteins in a concentration-dependent manner without heat treatment and also after heat treatment at 75 and 100 °C, and the effect was enhanced after storage under either ambient or refrigerated storage conditions. Interactions of wPRP and milk proteins were monitored by particle size analysis and tryptic digestion and specifically linked with solubilisation of αS1 casein (αS1-Cn), which supported observed changes in milk protein solubility. The results suggested that wPRP preferably prevented or reversed physical versus covalent protein aggregation, with the relaxation of hydrophobic interactions at 4 °C providing an additive effect. This application of wPRP represents a novel approach to stabilisation of dairy proteins following thermal processing with industrial usefulness yet to be explored.

The ability of Trichomonas vaginalis to adhere to plastic surfaces in the presence of various agents and under different growth conditions was examined in wells of microtitre plates containing unsupplemented TYI medium or the same, with various supplements. Following incubation, the wells were thoroughly washed and adhesion was determined by microscopic counting of the adherent organisms. There was no detectable adhesion in the absence of both serum and carbohydrate. Optimal adhesion (about 10–20% of the total number of parasites) was obtained throughout the growth curve in culture media supplemented with either serum or serum Cohn fractions IV–I (rich in α-globulin) or IV-4 (rich in α + β-globulin) and 25 mM glucose, maltose or fructose, but not in plates pre-coated with the Cohn fractions. Cohn fraction II + III (rich in β + γ-globulin) moderately enhanced adhesion while Cohn fractions II (rich in γ-globulin) or V (albumin), fibronectin, Tamm-Horsfall glycoproteins and polylysine were without effect. Non-metabolizable sugars (methyl derivatives of glucose, mannose or fucose) did not support growth, but, surprisingly, enhanced adhesion. At 4 °C, the trichomonads were not able to adhere and pre-adherent organisms detached from the plastic surface. Optimal adhesion was obtained at a pH range of 6·5–7·5 but was already detectable at pH 5·5. Cytochalasin E markedly suppressed adhesion. The data taken together suggest that the firm, serum-dependent adhesion of T. vaginalis to plastic surfaces is apparently not influenced by the rate of multiplication, requires energy and the binding by the organisms of certain serum proteins, which possibly enhances their hydrophobic interaction with the plastic substratum.